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Bacterial Na(+)-ATP synthase has an undecameric rotor
H Stahlberg1, D J Müller, K Suda
1M.E. Müller Institute for Structural Biology, Biozentrum, University of Basel, Klingelbergstrasse 70, CH-4056 Basel, Switzerland.
EMBO Reports
|March 27, 2001
Summary
The F(0) ATP synthase rotor uses a sodium-driven mechanism. Researchers found that the Ilyobacter tartaricus ATP synthase rotor contains 11 c-subunits, differing from yeast and chloroplast ATP synthases.
Area of Science:
- Biochemistry
- Structural Biology
- Microbiology
Background:
- Adenosine triphosphate (ATP) synthase is a crucial enzyme for cellular energy production.
- The F(0) domain acts as a membrane-embedded rotary engine driving ATP synthesis.
- The rotor component of F(0) is composed of multiple c-subunits.
Purpose of the Study:
- To determine the rotor stoichiometry of Ilyobacter tartaricus ATP synthase.
- To investigate the structural basis of sodium-driven ATP synthesis in this organism.
Main Methods:
- Atomic force microscopy (AFM) was employed to visualize the ATP synthase complex.
- Cryo-electron microscopy (cryo-EM) provided high-resolution structural details.
- Analysis of rotor composition and subunit arrangement.
Main Results:
- The cylindrical rotor of Ilyobacter tartaricus ATP synthase was shown to contain 11 c-subunits.
- This stoichiometry differs from previously characterized ATP synthases, such as yeast (10 subunits) and chloroplasts (14 subunits).
- The rotor is driven by sodium ions, indicating a specific ion translocation mechanism.
Conclusions:
- The study elucidates the specific rotor stoichiometry of Ilyobacter tartaricus ATP synthase.
- Findings contribute to understanding the diversity of ATP synthase structures and mechanisms.
- This research provides insights into the evolution and adaptation of energy-transducing machinery.